Evidence map›Paper›PMID 39906902›Full record

ArticleCell reports. Physical science2024

Label-free electronic detection of peptide post-translational modification with functional enzyme-driven assay at the physical limit.

Eleonora Macchia, Kim Björkström, Amit Tewari, Ville Eskonen, Axel Luukkonen, Amir Mohammad Ghafari, Lucia Sarcina, Mariapia Caputo, Natalia Tong-Ochoa, Kari Kopra and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports. Physical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors.

Eleonora MacchiaPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Kim BjörkströmPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Amit TewariPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Ville EskonenChemistry of Drug Development, Department of Chemistry, University of Turku, 20500 Turku, Finland.
Axel LuukkonenPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Amir Mohammad GhafariPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Lucia SarcinaDipartimento di Chimica, Università degli Studi di Bari Aldo Moro, 70125 Bari, Italy.
Mariapia CaputoDepartment of Pharmaceutical Sciences, Università degli Studi di Bari Aldo Moro, 70125 Bari, Italy.
Natalia Tong-OchoaChemistry of Drug Development, Department of Chemistry, University of Turku, 20500 Turku, Finland.
Kari KopraChemistry of Drug Development, Department of Chemistry, University of Turku, 20500 Turku, Finland.
Fredrik PetterssonPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Zahra GounaniPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.
Luisa TorsiDipartimento di Chimica, Università degli Studi di Bari Aldo Moro, 70125 Bari, Italy.
Harri HärmäChemistry of Drug Development, Department of Chemistry, University of Turku, 20500 Turku, Finland.
Ronald ÖsterbackaPhysics and Center for Functional Materials, Faculty of Science and Engineering, Åbo Akademi University, 20500 Turku, Finland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-performance, ultra-sensitive, and universal protein post-translational modification (PTM) and protein-protein interaction (PPI) technologies are eagerly pursued in the pharmaceutical industry and bioanalytical research. Novel PTM and PPI detection methods outperform traditional assays in scope and scalability, enabling the collection of information on multiple biochemical targets. Detecting peptides and proteins at the single-molecule level is done by utilizing nanosized transducing elements and assaying solutions at very high analyte concentrations, in the nanomolar range or higher. Here, a proof of principle of a biosensing platform for single-molecule PTM detection is demonstrated. This platform is based on the single molecule with a large transistor (SiMoT) technology, encompassing a millimeter-sized electrolyte-gated organic field-effect transistor, for label-free PTM detection with a zeptomolar limit of detection. Sensitivity is improved 10

Indexed as

multivariate data processingorganic bioelectronicspeptide detectionSiMoTsingle-molecule assay with large transistorssingle-molecule detection

Identifiers

PMID39906902
PMCPMC11791991

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.